We are interested in investigating several mutants of the green fluorescent protein (GFP) which have specific amino acid mutations near the natural fluorescent chromophore. These mutations will allow us to probe various non radiative processes (charge transfer, etc.) as well as their effect on the radiative lifetimes. We are also interested in investigating the details of the folding dynamics of these proteins. GFPs have a reasonably sharp melting curve and thus the large temperature jumps available on the instrument at the RLBL would serve us well as a trigger for the folding dynamic process, which would be monitored by the change in fluorescence of the GFPs